dbPTM

CDN1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CDN1B_HUMAN
UniProt AC	P46527
Protein Name	Cyclin-dependent kinase inhibitor 1B
Gene Name	CDKN1B
Organism	Homo sapiens (Human).
Sequence Length	198
Subcellular Localization	Nucleus. Cytoplasm. Endosome. Nuclear and cytoplasmic in quiescent cells. AKT- or RSK-mediated phosphorylation on Thr-198, binds 14-3-3, translocates to the cytoplasm and promotes cell cycle progression. Mitogen-activated UHMK1 phosphorylation on Ser
Protein Description	Important regulator of cell cycle progression. Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA. [PubMed: 28666995 Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry.]
Protein Sequence	MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	O-linked_Glycosylation	------MSNVRVSNG ------CCCCCCCCC	43.99	111190599
2	Phosphorylation	------MSNVRVSNG ------CCCCCCCCC	43.99	23403867
7	Phosphorylation	-MSNVRVSNGSPSLE -CCCCCCCCCCCCHH	25.55	30266825
10	Phosphorylation	NVRVSNGSPSLERMD CCCCCCCCCCHHHHH	18.63	29255136
12	Phosphorylation	RVSNGSPSLERMDAR CCCCCCCCHHHHHHH	44.55	30266825
15	Methylation	NGSPSLERMDARQAE CCCCCHHHHHHHHCC	33.31	24151417
25	Ubiquitination	ARQAEHPKPSACRNL HHHCCCCCCHHHHHH	54.21	-
68	Ubiquitination	NFDFQNHKPLEGKYE CCCCCCCCCCCCCCE	59.87	-
74	Phosphorylation	HKPLEGKYEWQEVEK CCCCCCCCEEEEEHH	33.00	19204084
81	Acetylation	YEWQEVEKGSLPEFY CEEEEEHHCCCCCEE	60.00	7959773
81	Ubiquitination	YEWQEVEKGSLPEFY CEEEEEHHCCCCCEE	60.00	-
83	Phosphorylation	WQEVEKGSLPEFYYR EEEEHHCCCCCEECC	52.39	15034923
88	Phosphorylation	KGSLPEFYYRPPRPP HCCCCCEECCCCCCC	9.26	19204084
89	Phosphorylation	GSLPEFYYRPPRPPK CCCCCEECCCCCCCC	23.20	18454177
100	Acetylation	RPPKGACKVPAQESQ CCCCCCCCCCCCCCC	51.20	22547391
106	Phosphorylation	CKVPAQESQDVSGSR CCCCCCCCCCCCCCC	21.43	26437602
106	O-linked_Glycosylation	CKVPAQESQDVSGSR CCCCCCCCCCCCCCC	21.43	144407
110	Phosphorylation	AQESQDVSGSRPAAP CCCCCCCCCCCCCCC	39.06	28348404
110	O-linked_Glycosylation	AQESQDVSGSRPAAP CCCCCCCCCCCCCCC	39.06	111190603
112	Phosphorylation	ESQDVSGSRPAAPLI CCCCCCCCCCCCCCC	27.82	28348404
134	Ubiquitination	DTHLVDPKTDPSDSQ CCCCCCCCCCCCCCC	62.18	10318797
135	Phosphorylation	THLVDPKTDPSDSQT CCCCCCCCCCCCCCC	59.54	27251275
138	Phosphorylation	VDPKTDPSDSQTGLA CCCCCCCCCCCCCHH	53.34	27251275
140	Phosphorylation	PKTDPSDSQTGLAEQ CCCCCCCCCCCHHHH	33.70	23401153
142	Phosphorylation	TDPSDSQTGLAEQCA CCCCCCCCCHHHHHH	37.81	27251275
153	Ubiquitination	EQCAGIRKRPATDDS HHHHCCCCCCCCCCC	61.89	10318797
154	Methylation	QCAGIRKRPATDDSS HHHCCCCCCCCCCCC	19.08	30762713
154	Dimethylation	QCAGIRKRPATDDSS HHHCCCCCCCCCCCC	19.08	-
157	O-linked_Glycosylation	GIRKRPATDDSSTQN CCCCCCCCCCCCHHC	42.92	10137
157	Phosphorylation	GIRKRPATDDSSTQN CCCCCCCCCCCCHHC	42.92	15280662
165	Ubiquitination	DDSSTQNKRANRTEE CCCCHHCHHHCCCCC	42.97	22053931
170	Phosphorylation	QNKRANRTEENVSDG HCHHHCCCCCCCCCC	47.67	23403867
175	Phosphorylation	NRTEENVSDGSPNAG CCCCCCCCCCCCCCC	48.08	25849741
178	Phosphorylation	EENVSDGSPNAGSVE CCCCCCCCCCCCCCC	21.70	23401153
183	Phosphorylation	DGSPNAGSVEQTPKK CCCCCCCCCCCCCCC	21.77	23403867
187	Phosphorylation	NAGSVEQTPKKPGLR CCCCCCCCCCCCCCC	24.46	10931950
198	O-linked_Glycosylation	PGLRRRQT------- CCCCCCCC-------	38.47	17177
198	Phosphorylation	PGLRRRQT------- CCCCCCCC-------	38.47	15280662

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
10	S	Phosphorylation	Kinase	KIS	Q8TAS1	PSP
10	S	Phosphorylation	Kinase	RPS6KA3	P18654	GPS
10	S	Phosphorylation	Kinase	RPS6KA1	Q63531	GPS
10	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
10	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
10	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
10	S	Phosphorylation	Kinase	CDK6	Q00534	PSP
10	S	Phosphorylation	Kinase	CDK16	Q00536	PSP
10	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
10	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
10	S	Phosphorylation	Kinase	AKT1	P31749	PSP
74	Y	Phosphorylation	Kinase	YES1	P07947	GPS
74	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
74	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
83	S	Phosphorylation	Kinase	CSNK2B	-	GPS
83	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
88	Y	Phosphorylation	Kinase	JAK2	O60674	Uniprot
88	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
88	Y	Phosphorylation	Kinase	LYN	P07948	Uniprot
88	Y	Phosphorylation	Kinase	LYN	P25911	PSP
88	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
88	Y	Phosphorylation	Kinase	ABL	P00520	PSP
88	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
88	Y	Phosphorylation	Kinase	YES1	P07947	GPS
88	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
89	Y	Phosphorylation	Kinase	SRC	P12931	PSP
89	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
89	Y	Phosphorylation	Kinase	YES1	P07947	GPS
89	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
140	S	Phosphorylation	Kinase	ATM	Q13315	PSP
140	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
157	T	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
157	T	Phosphorylation	Kinase	PIM1	P11309	Uniprot
157	T	Phosphorylation	Kinase	SGK1	O00141	PSP
157	T	Phosphorylation	Kinase	AKT1	P31749	Uniprot
157	T	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
157	T	Phosphorylation	Kinase	CAMK1A	Q14012	PSP
178	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
187	T	Phosphorylation	Kinase	AKT1	P31749	Uniprot
187	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
187	T	Phosphorylation	Kinase	CDK2	P24941	Uniprot
187	T	Phosphorylation	Kinase	CDK2	P97377	PSP
187	T	Phosphorylation	Kinase	CDK6	Q00534	PSP
187	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
187	T	Phosphorylation	Kinase	ABL	P00519	PSP
187	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
198	T	Phosphorylation	Kinase	RSK_GROUP	-	PhosphoELM
198	T	Phosphorylation	Kinase	RPS6KA3	P18654	GPS
198	T	Phosphorylation	Kinase	RSK-SUBFAMILY	-	GPS
198	T	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
198	T	Phosphorylation	Kinase	AKT1	P31749	Uniprot
198	T	Phosphorylation	Kinase	CAMK1A	Q14012	PSP
198	T	Phosphorylation	Kinase	RPS6KA1	Q15418	Uniprot
198	T	Phosphorylation	Kinase	SGK1	O00141	PSP
198	T	Phosphorylation	Kinase	PIM1	P11309	Uniprot
198	T	Phosphorylation	Kinase	RPS6KA1	Q63531	GPS
198	T	Phosphorylation	Kinase	KS6A3	P51812	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	CDC34	P49427	PMID:19123975
-	K	Ubiquitination	E3 ubiquitin ligase	UBE3A	Q05086	PMID:19591933
-	K	Ubiquitination	E3 ubiquitin ligase	COP1	Q8NHY2	PMID:26254224
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:10375532
-	K	Ubiquitination	E3 ubiquitin ligase	RCHY1	Q96PM5	PMID:18006823
-	K	Ubiquitination	E3 ubiquitin ligase	CDC20	Q12834	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM21	P19474	PMID:10323868
-	K	Ubiquitination	E3 ubiquitin ligase	RNF123	Q5XPI4	PMID:15531880
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH2	O43255	PMID:21734459
-	K	Ubiquitination	E3 ubiquitin ligase	SAG	P10523	PMID:23136067
-	K	Ubiquitination	E3 ubiquitin ligase	WWP1	Q9H0M0	PMID:21795702

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
10	S	Phosphorylation	10831586
Phosphorylation on Ser-10 is the major site of phosphorylation in resting cells, takes place at the G(0)-G(1) phase and leads to protein stability.
187	T	Phosphorylation	10323868
Phosphorylation on Thr-187, by CDK1 and CDK2 leads to protein ubiquitination and proteasomal degradation.
187	T	Phosphorylation	10323868
The latter requires prior phosphorylation on Thr-187.
187	T	ubiquitylation	10323868
Phosphorylation on Thr-187, by CDK1 and CDK2 leads to protein ubiquitination and proteasomal degradation.
198	T	Phosphorylation	12042314
Phosphorylation on Thr-198 is required for interaction with 14-3-3 proteins.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of CDN1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NUP50_HUMAN	NUP50	physical	10891500
TRAF2_HUMAN	TRAF2	physical	16189514
SPDYA_HUMAN	SPDYA	physical	12972555
UCHL1_HUMAN	UCHL1	physical	12082530
CDK6_HUMAN	CDK6	physical	11360184
CCND3_HUMAN	CCND3	physical	11360184
CDK4_HUMAN	CDK4	physical	11360184
CCND1_HUMAN	CCND1	physical	11360184
CCND3_HUMAN	CCND3	physical	10342870
XPO1_HUMAN	XPO1	physical	11889117
SKP2_HUMAN	SKP2	physical	12042314
AKT1_HUMAN	AKT1	physical	12042314
1433T_HUMAN	YWHAQ	physical	12042314
GRB2_HUMAN	GRB2	physical	11278754
XPO1_HUMAN	XPO1	physical	12529437
CCNE1_HUMAN	CCNE1	physical	12529437
CDK2_HUMAN	CDK2	physical	12529437
CUL4A_HUMAN	CUL4A	physical	19056892
CCNA1_HUMAN	CCNA1	physical	16774918
CSN5_HUMAN	COPS5	physical	16951171
SKP2_HUMAN	SKP2	physical	15735731
UBAC1_HUMAN	UBAC1	physical	15531880
RN123_HUMAN	RNF123	physical	15531880
SKP2_HUMAN	SKP2	physical	15469821
CCND3_HUMAN	CCND3	physical	10597239
DDB1_HUMAN	DDB1	physical	21237244
SKP2_HUMAN	SKP2	physical	21237244
UBE3A_HUMAN	UBE3A	physical	19591933
PIN1_HUMAN	PIN1	physical	19584057
CKS1_HUMAN	CKS1B	physical	19584057
PIN1_MOUSE	Pin1	physical	19584057
IMA3_HUMAN	KPNA4	physical	15057270
IMA5_HUMAN	KPNA1	physical	15057270
1433E_HUMAN	YWHAE	physical	15057270
KAT2B_HUMAN	KAT2B	physical	22547391
H15_HUMAN	HIST1H1B	physical	17671428
CDK2_HUMAN	CDK2	physical	12800980
CCNA2_HUMAN	CCNA2	physical	9724724
CDK2_HUMAN	CDK2	physical	9724724
CCNE1_HUMAN	CCNE1	physical	8891332
JAK2_HUMAN	JAK2	physical	21423214
CDK4_HUMAN	CDK4	physical	8978686
CDK2_HUMAN	CDK2	physical	8978686
CCND1_HUMAN	CCND1	physical	9311993
CCNA2_HUMAN	CCNA2	physical	9311993
CCNE1_HUMAN	CCNE1	physical	9311993
CDK2_HUMAN	CDK2	physical	9311993
CDK4_HUMAN	CDK4	physical	9311993
CUL4A_HUMAN	CUL4A	physical	16467204
SKP2_HUMAN	SKP2	physical	20160482
SKP2_HUMAN	SKP2	physical	15355997
CDK2_HUMAN	CDK2	physical	15355997
TSC1_HUMAN	TSC1	physical	15355997
TSC2_HUMAN	TSC2	physical	15355997
SKP2_HUMAN	SKP2	physical	10559916
SKP1_HUMAN	SKP1	physical	10559916
CUL1_HUMAN	CUL1	physical	10559916
ZN363_HUMAN	RCHY1	physical	21236467
CDK2_HUMAN	CDK2	physical	11940657
H11_HUMAN	HIST1H1A	physical	11940657
CCND1_HUMAN	CCND1	physical	11940657
CDK4_HUMAN	CDK4	physical	11940657
CCNE1_HUMAN	CCNE1	physical	11940657
CSN5_HUMAN	COPS5	physical	15480426
CSN5_HUMAN	COPS5	physical	18285702
CDK2_HUMAN	CDK2	physical	18285702
CDK4_HUMAN	CDK4	physical	18285702
CCND3_HUMAN	CCND3	physical	16782892
CDK4_HUMAN	CDK4	physical	16782892
CDK6_HUMAN	CDK6	physical	16782892
CDK2_HUMAN	CDK2	physical	16782892
MK08_HUMAN	MAPK8	physical	12963725
MK10_HUMAN	MAPK10	physical	12963725
CCNE1_HUMAN	CCNE1	physical	17254967
CDK2_HUMAN	CDK2	physical	17254967
SRC_HUMAN	SRC	physical	17254967
SKP2_HUMAN	SKP2	physical	18239684
CDK2_HUMAN	CDK2	physical	9660939
IMA7_HUMAN	KPNA6	physical	22770219
CCNE2_HUMAN	CCNE2	physical	9840943
CDK5_HUMAN	CDK5	physical	15890360
CDK2_HUMAN	CDK2	physical	15890360
KS6A1_HUMAN	RPS6KA1	physical	19470470
RHOA_HUMAN	RHOA	physical	19470470
CDK4_HUMAN	CDK4	physical	16326706
CDK2_HUMAN	CDK2	physical	16326706
CDK2_HUMAN	CDK2	physical	17053782
CDK4_HUMAN	CDK4	physical	17053782
CCND3_HUMAN	CCND3	physical	23718855
LYN_HUMAN	LYN	physical	17254966
CDK2_HUMAN	CDK2	physical	17254966
CCNA2_HUMAN	CCNA2	physical	17254966
1433T_HUMAN	YWHAQ	physical	17470459
TSC2_HUMAN	TSC2	physical	17470459
IRF1_HUMAN	IRF1	physical	21988832
PSB1_HUMAN	PSMB1	physical	23725357
CSN5_HUMAN	COPS5	physical	18202760
TXNIP_HUMAN	TXNIP	physical	18202760
CSN5_HUMAN	COPS5	physical	24671224
SKP2_HUMAN	SKP2	physical	21503567
RFWD2_HUMAN	RFWD2	physical	26254224
SKP2_HUMAN	SKP2	physical	26450989
CDK2_HUMAN	CDK2	physical	26450989
MYC_HUMAN	MYC	physical	26701207
HSP7C_HUMAN	HSPA8	physical	26775844
XPO1_HUMAN	XPO1	physical	27175940
CCNE1_HUMAN	CCNE1	physical	27175940
CDK2_HUMAN	CDK2	physical	27175940
CDK6_HUMAN	CDK6	physical	21439954
CDK4_HUMAN	CDK4	physical	21439954
CDK2_HUMAN	CDK2	physical	21439954
RHOA_HUMAN	RHOA	physical	23333463
VHL_HUMAN	VHL	genetic	28319113
IGF1R_HUMAN	IGF1R	genetic	28319113
SIR6_HUMAN	SIRT6	physical	27794562
GNL3_HUMAN	GNL3	physical	27998760
CSN5_HUMAN	COPS5	physical	28919423
AKT1_HUMAN	AKT1	physical	28919423

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610755	Multiple endocrine neoplasia 4 (MEN4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CDN1B_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal proteinS6 kinases promotes its binding to 14-3-3 and cytoplasmiclocalization."; Fujita N., Sato S., Tsuruo T.; J. Biol. Chem. 278:49254-49260(2003). Cited for: PHOSPHORYLATION AT SER-10 AND THR-198, INTERACTION WITH YWHAE; YWHAH;SFN; YWHAQ; RPS6KA1 AND RPS6KA3, SUBCELLULAR LOCATION, AND MUTAGENESISOF THR-157 AND THR-198.	14504289 [Abstract]
"Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3and cytoplasmic localization."; Fujita N., Sato S., Katayama K., Tsuruo T.; J. Biol. Chem. 277:28706-28713(2002). Cited for: PHOSPHORYLATION AT SER-10; THR-187 AND THR-198, INTERACTION WITH AKT1AND YWHAQ, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-10; THR-157;THR-187 AND THR-198.	12042314 [Abstract]
"A growth factor-dependent nuclear kinase phosphorylates p27(Kip1) andregulates cell cycle progression."; Boehm M., Yoshimoto T., Crook M.F., Nallamshetty S., True A.,Nabel G.J., Nabel E.G.; EMBO J. 21:3390-3401(2002). Cited for: INTERACTION WITH UHMK1, PHOSPHORYLATION AT SER-10, SUBCELLULARLOCATION, AND MUTAGENESIS OF SER-10 AND THR-187.	12093740 [Abstract]
"Phosphorylation at serine 10, a major phosphorylation site ofp27(Kip1), increases its protein stability."; Ishida N., Kitagawa M., Hatakeyama S., Nakayama K.; J. Biol. Chem. 275:25146-25154(2000). Cited for: PHOSPHORYLATION AT SER-10, AND FUNCTION.	10831586 [Abstract]
"Structural basis of the Cks1-dependent recognition of p27(Kip1) bythe SCF(Skp2) ubiquitin ligase."; Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M.,Pavletich N.P.; Mol. Cell 20:9-19(2005). Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 181-190 IN COMPLEX WITH SKP1;SKP2 AND CKS1B, PHOSPHORYLATION AT THR-187, MUTAGENESIS OF GLU-185 ANDTHR-187, AND UBIQUITINATION.	16209941 [Abstract]
"Pim kinases promote cell cycle progression by phosphorylating anddown-regulating p27Kip1 at the transcriptional and posttranscriptionallevels."; Morishita D., Katayama R., Sekimizu K., Tsuruo T., Fujita N.; Cancer Res. 68:5076-5085(2008). Cited for: INTERACTION WITH PIM1, AND PHOSPHORYLATION AT THR-157 AND THR-198.	18593906 [Abstract]
"Akt-dependent T198 phosphorylation of cyclin-dependent kinaseinhibitor p27kip1 in breast cancer."; Motti M.L., De Marco C., Califano D., Fusco A., Viglietto G.; Cell Cycle 3:1074-1080(2004). Cited for: PHOSPHORYLATION AT THR-198, SUBCELLULAR LOCATION, AND MUTAGENESIS OFSER-10; THR-157; THR-187 AND THR-198.	15280662 [Abstract]
"PKB/Akt mediates cell-cycle progression by phosphorylation ofp27(Kip1) at threonine 157 and modulation of its cellularlocalization."; Shin I., Yakes F.M., Rojo F., Shin N.-Y., Bakin A.V., Baselga J.,Arteaga C.L.; Nat. Med. 8:1145-1152(2002). Cited for: PHOSPHORYLATION AT THR-157, INTERACTION WITH AKT1, SUBCELLULARLOCATION, FUNCTION, AND MUTAGENESIS OF THR-157; SER-161 AND THR-162.	12244301 [Abstract]
"Cytoplasmic relocalization and inhibition of the cyclin-dependentkinase inhibitor p27(Kip1) by PKB/Akt-mediated phosphorylation inbreast cancer."; Viglietto G., Motti M.L., Bruni P., Melillo R.M., D'Alessio A.,Califano D., Vinci F., Chiappetta G., Tsichlis P., Bellacosa A.,Fusco A., Santoro M.; Nat. Med. 8:1136-1144(2002). Cited for: PHOSPHORYLATION AT THR-157, SUBCELLULAR LOCATION, ASSOCIATION WITHBREAST CANCER, AND MUTAGENESIS OF THR-157.	12244303 [Abstract]
"Cdk-inhibitory activity and stability of p27Kip1 are directlyregulated by oncogenic tyrosine kinases."; Grimmler M., Wang Y., Mund T., Cilensek Z., Keidel E.-M.,Waddell M.B., Jaekel H., Kullmann M., Kriwacki R.W., Hengst L.; Cell 128:269-280(2007). Cited for: STRUCTURE BY NMR OF 22-104, PHOSPHORYLATION AT TYR-88, FUNCTION,INDUCTION, INTERACTION WITH LYN, MASS SPECTROMETRY, AND MUTAGENESIS OFTYR-88 AND TYR-89.	17254966 [Abstract]
"Tyrosine phosphorylation modulates binding preference to cyclin-dependent kinases and subcellular localization of p27Kip1 in the acutepromyelocytic leukemia cell line NB4."; Kardinal C., Dangers M., Kardinal A., Koch A., Brandt D.T., Tamura T.,Welte K.; Blood 107:1133-1140(2006). Cited for: PHOSPHORYLATION AT TYR-88 AND TYR-89, DEPHOSPHORYLATION, INTERACTIONWITH GRB2; CDK2 AND CDK4, SUBCELLULAR LOCATION, AND MUTAGENESIS OFTYR-74; TYR-88 AND TYR-89.	16195327 [Abstract]

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